Search results for "DOMAINS"

showing 10 items of 269 documents

Targeting SARS-CoV-2 RBD Interface: a Supervised Computational Data-Driven Approach to Identify Potential Modulators

2020

Coronavirus disease 2019 (COVID-19) has spread out as a pandemic threat affecting over 2 million people. The infectious process initiates via binding of SARS-CoV-2 Spike (S) glycoprotein to host angiotensin-converting enzyme 2 (ACE2). The interaction is mediated by the receptor-binding domain (RBD) of S glycoprotein, promoting host receptor recognition and binding to ACE2 peptidase domain (PD), thus representing a promising target for therapeutic intervention. Herein, we present a computational study aimed at identifying small molecules potentially able to target RBD. Although targeting PPI remains a challenge in drug discovery, our investigation highlights that interaction between SARS-CoV…

Protein domainPneumonia ViralDruggabilityDrug Evaluation Preclinicalprotein-protein interactionsComputational biologyBiologyMolecular Dynamics SimulationPeptidyl-Dipeptidase AMolecular dynamics01 natural sciencesBiochemistryMolecular Docking SimulationAntiviral Agentsdockingmolecular dynamicProtein–protein interactionSmall Molecule LibrariesBetacoronavirusProtein DomainsDrug DiscoveryHumansGeneral Pharmacology Toxicology and PharmaceuticsPandemicsPharmacologyFull Paperpharmacophore010405 organic chemistryDrug discoverySARS-CoV-2Organic ChemistryCOVID-19Small molecule0104 chemical sciencesProtein-Protein InteractionMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)Spike Glycoprotein CoronavirusdockingMolecular MedicineAngiotensin-Converting Enzyme 2PharmacophoreCoronavirus InfectionsProtein Binding
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Membrane vesicles containing matrix metalloproteinase-9 and fibroblast growth factor-2 are released into the extracellular space from mouse mesoangio…

2010

Certain proteins, including fibroblast growth factor-2 (FGF-2) and matrix metalloproteinase-9 (MMP-9), have proved very effective in increasing the efficacy of mesoangioblast stem cell therapy in repairing damaged tissue. We provide the first evidence that mouse mesoangioblast stem cells release FGF-2 and MMP-9 in their active form through the production of membrane vesicles. These vesicles are produced and turned over continuously, but are stable for some time in the extracellular milieu. Mesoangioblasts shed membrane vesicles even under oxygen tensions that are lower than those typically used for cell culture and more like those of mouse tissues. These findings suggest that mesoangioblast…

ProteomicsTime FactorsPhysiologyClinical BiochemistryBiologyFibroblast growth factorCell LineMiceMembrane MicrodomainsTubulinParacrine CommunicationmedicineExtracellularAnimalsSecretionSettore BIO/06 - Anatomia Comparata E CitologiaFibroblastCytoskeletonMembrane vesicles MMP9 FGF2 mouse mesoangioblastMesoangioblastSecretory VesiclesVesicleBiological TransportMesenchymal Stem CellsCell BiologyCell biologyOxygenmedicine.anatomical_structureMatrix Metalloproteinase 9Cell cultureFibroblast Growth Factor 2Stem cellExtracellular Space
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Geometric Properties of Planar BV -Extension Domains

2009

We investigate geometric properties of those planar domains that are extension for functions with bounded variation.We start from a characterization of such domains given by Burago–Maz'ya and prove that a bounded, simply connected domain is a BV -extension domain if and only if its com- plement is quasiconvex. We further prove that the extension property is a bi-Lipschitz invariant and give applications to Sobolev extension domains.

Discrete mathematicsQuasiconformal mappingMathematics::Analysis of PDEsGeometric propertySobolev spaceQuasiconvex functionExtension domains; Sobolev spaces; Functions with bounded variationPlanarSobolev spacesFunctions with bounded variationBounded functionSimply connected spaceInvariant (mathematics)Extension domainsMathematics
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Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features

2020

Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) that is engendering the severe coronavirus disease 2019 (COVID-19) pandemic. The spike (S) protein receptor-binding domain (RBD) of SARS-CoV-2 binds to the three sub-domains viz. amino acids (aa) 22&ndash

Pan troglodytesvirusesProtein domainACE2Pharmaceutical ScienceBiologyArticleAnalytical Chemistrylcsh:QD241-44103 medical and health sciencesDogs0302 clinical medicineProtein DomainsSpecies Specificitylcsh:Organic chemistryDrug DiscoveryAnimalsHumansviral spike receptor-binding domainPhysical and Theoretical ChemistryReceptor030304 developmental biologychemistry.chemical_classification0303 health sciencesCATSSARS-CoV-2Transmission (medicine)fungiOrganic ChemistrytransmissionCOVID-19virus diseasesbioinformaticsMetabolismVirologyAmino acidEnzymechemistryChemistry (miscellaneous)030220 oncology & carcinogenesisSpike Glycoprotein CoronavirusAngiotensin-converting enzyme 2CatsMolecular MedicineCattleAngiotensin-Converting Enzyme 2hormones hormone substitutes and hormone antagonistsMolecules
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Comparative lipidomics and proteomics analysis of platelet lipid rafts using different detergents

2016

Lipid rafts play a pivotal role in physiological functions of platelets. Their isolation using nonionic mild detergents is considered as the gold standard method, but there is no consensual detergent for lipid raft studies. We aimed to investigate which detergent is the most suitable for lipid raft isolation from platelet membrane, based on lipidomics and proteomics analysis. Platelets were obtained from healthy donors. Twelve sucrose fractions were extracted by three different detergents, namely Brij 35, Lubrol WX, and Triton X100, at 0.05% and 1%. After lipidomics analysis and determination of fractions enriched in cholesterol (Ch) and sphingomyelin (SM), proteomics analysis was performed…

Blood Platelets0301 basic medicineProteome[SDV]Life Sciences [q-bio]Detergents030204 cardiovascular system & hematologyProteomics03 medical and health scienceschemistry.chemical_compoundMembrane Microdomains0302 clinical medicineproteomicsLipidomicsCentrifugation Density GradientHumansLipid raftlipid rafts[ SDV ] Life Sciences [q-bio]ChemistryCholesterolMembrane ProteinsHematologyGeneral MedicineLipids6. Clean water030104 developmental biologyMembraneBiochemistryMembrane proteinProteomeplateletslipidomicslipids (amino acids peptides and proteins)Sphingomyelin
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Evaluation of web reinforcements in prestressed concrete box girders through shear-transverse bending domains

2020

In concrete box girders, the amount and distribution of reinforcements in the webs have to be estimated considering the local effects due to eccentric external loads and cross-sectional distortion and not only the global effect due to the resultant forces of a longitudinal analysis: shear, torsion and bending. This work presents an analytical model that allows designers to take into account the interaction of all these effects, global and local, for the determination of the reinforcements. The model is based on the theory of stress fields and it has been compared to a 3D finite element analysis, in order to validate the interaction domains. The results show how the proposed analytical mode…

thin-walled section0211 other engineering and technologies020101 civil engineeringbox girders bridges; interaction domains; prestressed concrete; shear; thin-walled section; transverse bending; web reinforcement02 engineering and technologyshear0201 civil engineeringlaw.inventionPrestressed concretelawGirder021105 building & constructionbox girders bridgesReinforcementCivil and Structural Engineeringinteraction domainsbusiness.industryprestressed concreteweb reinforcementtransverse bendingBuilding and ConstructionStructural engineeringSettore ICAR/09 - Tecnica Delle CostruzioniShear (geology)Transverse shear deformationbusinessGeology
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2018

Tetraspanins (Tspans) are a family of four-span transmembrane proteins, known as plasma membrane “master organizers.” They form Tspan-enriched microdomains (TEMs or TERMs) through lateral association with one another and other membrane proteins. If multiple microdomains associate with each other, larger platforms can form. For infection, viruses interact with multiple cell surface components, including receptors, activating proteases, and signaling molecules. It appears that Tspans, such as CD151, CD82, CD81, CD63, CD9, Tspan9, and Tspan7, coordinate these associations by concentrating the interacting partners into Tspan platforms. In addition to mediating viral attachment and entry, these …

lcsh:Immunologic diseases. Allergy0301 basic medicineCell signalingTetraspaninsMini ReviewreceptorImmunology610 MedizinbuddingvirusBiologyVirusStructure-Activity Relationship03 medical and health sciencesMembrane MicrodomainsTetraspanintrafficking610 Medical sciencesAnimalsHumansendocytosisImmunology and Allergy030102 biochemistry & molecular biologymicrodomainLipid microdomainMembrane ProteinsVirus InternalizationTransmembrane proteinCell biologytetraspanin030104 developmental biologyMembrane proteinViral replicationVirus DiseasesHost-Pathogen Interactionsentrylcsh:RC581-607BiomarkersCD81Frontiers in Immunology
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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Thickness measurement of soft thin films on periodically patterned magnetic substrates by phase difference magnetic force microscopy

2013

The need for accurate measurement of the thickness of soft thin films is continuously encouraging the development of techniques suitable for this purpose. We propose a method through which the thickness of the film is deduced from the quantitative measurement of the contrast in the phase images of the sample surface acquired by magnetic force microscopy, provided that the film is deposited on a periodically patterned magnetic substrate. The technique is demonstrated by means of magnetic substrates obtained from standard floppy disks. Colonies of Staphylococcus aureus adherent to such substrates were used to obtain soft layers with limited lateral (a levy microns) and vertical (hundreds of n…

Staphylococcus aureusCantileverMaterials scienceThickness measurementMagnetic domainSurface PropertiesMicroscopy Atomic ForceAtomic force microscopyOpticsPeriodic magnetic domainsHomogeneity (physics)Thin filmInstrumentationDetection limitPhase differenceBacteriabusiness.industryMagnetic PhenomenaThickness measurement Magnetic force microscopy Atomic force microscopy Periodic magnetic domains BacteriaAtomic and Molecular Physics and OpticsElectronic Optical and Magnetic MaterialsMagnetic force microscopyatomic force microscopy; bacteria; magnetic force microscopy; periodic magnetic domains; thickness measurementNanometreMagnetic force microscopebusiness
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Water-Soluble Chlorophyll Protein (WSCP) Stably Binds Two or Four Chlorophylls

2017

Water-soluble chlorophyll proteins (WSCPs) of class IIa from Brassicaceae form tetrameric complexes containing one chlorophyll (Chl) per apoprotein but no carotenoids. The complexes are remarkably stable toward dissociation and protein denaturation even at 100 °C and extreme pH values, and the Chls are partially protected against photooxidation. There are several hypotheses that explain the biological role of WSCPs, one of them proposing that they function as a scavenger of Chls set free upon plant senescence or pathogen attack. The biochemical properties of WSCP described in this paper are consistent with the protein acting as an efficient and flexible Chl scavenger. At limiting Chl concen…

ChlorophyllModels Molecular0106 biological sciences0301 basic medicineProtein DenaturationHot TemperatureLightLight-Harvesting Protein ComplexesGene ExpressionThylakoids01 natural sciencesBiochemistryProtein Structure SecondaryDissociation (chemistry)law.inventionchemistry.chemical_compoundlawpolycyclic compoundsDenaturation (biochemistry)CarotenoidPlant Proteinschemistry.chemical_classificationSinglet OxygenProtein Stabilityfood and beveragesHydrogen-Ion ConcentrationBiochemistryRecombinant DNAOxidation-ReductionProtein BindingRecombinant Fusion ProteinsBrassicamacromolecular substancesBiology03 medical and health sciencesProtein DomainsTetramerPlant senescenceChlorophyll APeasWaterOxygen030104 developmental biologyWater solubleSolubilitychemistryChlorophyllProtein MultimerizationApoproteins010606 plant biology & botanyBiochemistry
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